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6LSR

Cryo-EM structure of a pre-60S ribosomal subunit - state B

This is a non-PDB format compatible entry.
Summary for 6LSR
Entry DOI10.2210/pdb6lsr/pdb
EMDB information0963
DescriptorZinc finger protein 622, 60S ribosomal protein L29, 60S ribosomal protein L4, ... (50 entities in total)
Functional Keywords60s, pre-60s, pre-ribosome, human 60s, human pre-ribosome, nmd3, human nmd3, ribosome
Biological sourceHomo sapiens (Human)
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Total number of polymer chains48
Total formula weight2808893.94
Authors
Liang, X.,Zuo, M.,Zhang, Y.,Li, N.,Ma, C.,Dong, M.,Gao, N. (deposition date: 2020-01-20, release date: 2020-08-26, Last modification date: 2025-04-09)
Primary citationLiang, X.,Zuo, M.Q.,Zhang, Y.,Li, N.,Ma, C.,Dong, M.Q.,Gao, N.
Structural snapshots of human pre-60S ribosomal particles before and after nuclear export.
Nat Commun, 11:3542-3542, 2020
Cited by
PubMed Abstract: Ribosome biogenesis is an elaborate and energetically expensive program that involve two hundred protein factors in eukaryotes. Nuclear export of pre-ribosomal particles is one central step which also serves as an internal structural checkpoint to ensure the proper completion of nuclear assembly events. Here we present four structures of human pre-60S particles isolated through a nuclear export factor NMD3, representing assembly stages immediately before and after nuclear export. These structures reveal locations of a dozen of human factors, including an uncharacterized factor TMA16 localized between the 5S RNA and the P0 stalk. Comparison of these structures shows a progressive maturation for the functional regions, such as peptidyl transferase centre and peptide exit tunnel, and illustrate a sequence of factor-assisted rRNA maturation events. These data facilitate our understanding of the global conservation of ribosome assembly in eukaryotes and species-specific features of human assembly factors.
PubMed: 32669547
DOI: 10.1038/s41467-020-17237-x
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.13 Å)
Structure validation

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